title: Anchors aweigh: protein localization and transport mediated by transmembrane domains.
abstract: The transmembrane domains (TMDs) of integral membrane proteins have emerged as major determinants of intracellular localization and transport in the secretory and endocytic pathways. Unlike sorting signals in cytosolic domains, TMD sorting determinants are not conserved amino acid sequences but physical properties such as the length and hydrophilicity of the transmembrane span. The underlying sorting machinery is still poorly characterized, but several mechanisms have been proposed, including TMD recognition by transmembrane sorting receptors and partitioning into membrane lipid domains. Here we review the nature of TMD sorting determinants and how they may dictate transmembrane protein localization and transport.
authors.affiliation: Département de Physiologie Cellulaire et Métabolisme, Centre Médical Universitaire, 1 rue Michel Servet, 1211 Geneva 4, Switzerland. Electronic address: Pierre.Cosson@unige.ch.
authors.forename: Pierre
authors.initials: P
authors.lastname: Cosson
authors.forename: Jackie
authors.initials: J
authors.lastname: Perrin
authors.forename: Juan S
authors.initials: JS
authors.lastname: Bonifacino
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D006056:Golgi Apparatus / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary / Q000235:genetics*; D021381:Protein Transport / Q000235:genetics*
chemical_list: D008565:Membrane Proteins
keywords: endomembrane system; lipid domains; protein sorting; protein traffic; transmembrane domains; transmembrane receptors